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• W1608043654 abstract "The interaction between troponin I and troponin C plays a critical role in the regulation of muscle contraction. In this study the interaction between troponin C (TnC) and the N-terminal region of TnI was investigated by the synthesis of three TnI peptides (residues 1-40/Rp, 10-40, and 20-40). The regulatory peptide (Rp) on binding to TnC prevents the ability of TnC to release the inhibition of the acto-S1-tropomyosin ATPase activity caused by TnI or the TnI inhibitory peptide (Ip), residues 104-115. A stable complex between TnC and Rp in the presence of Ca2+ was demonstrated by polyacrylamide gel electrophoresis in the presence of 6 M urea. Rp was able to displace TnI from a preformed TnI.TnC complex. In the absence of Ca2+, Rp was unable to maintain a complex with TnC in benign conditions of polyacrylamide gel electrophoresis which demonstrates the Ca(2+)-dependent nature of this interaction. Size-exclusion chromatography demonstrated that the TnC.Rp complex consisted of a 1:1 complex. The results of these studies have shown that the N-terminal region of TnI (1-40) plays a critical role in modulating the Ca(2+)-sensitive release of TnI inhibition by TnC." @default.
• W1608043654 created "2016-06-24" @default.
• W1608043654 creator A5052295449 @default.
• W1608043654 creator A5031426868 @default.
• W1608043654 date "1992-08-01" @default.
• W1608043654 modified "2023-10-16" @default.
• W1608043654 title "Biologically important interactions between synthetic peptides of the N-terminal region of troponin I and troponin C." @default.
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• W1608043654 doi "https://doi.org/10.1016/s0021-9258(19)49594-x" @default.
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